Literature DB >> 2645301

Detection of a specific isoform of alpha-actinin with antisera directed against dystrophin.

E P Hoffman1, S C Watkins, H S Slayter, L M Kunkel.   

Abstract

We have characterized a protein immunologically related to dystrophin, the protein product of the Duchenne muscular dystrophy gene. We identify this related protein as a fast-twitch glycolytic isoform (mouse extensor digitorum longus-specific) of myofibrillar alpha-actinin. This specific isoform of alpha-actinin exhibits a more restricted pattern of expression in skeletal muscle than fast-twitch-specific isoforms of both myosin and Ca2+-ATPase. Our results provide evidence that dystrophin and myofibrillar alpha-actinin are related proteins, reinforcing the previous data concerning the sequence homologies noted between nonmuscle cytoskeletal alpha-actinin and dystrophin. In addition, we describe the first antisera directed against a specific myofibrillar skeletal muscle isoform of alpha-actinin.

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Year:  1989        PMID： 2645301      PMCID： PMC2115443          DOI： 10.1083/jcb.108.2.503

Source DB:  PubMed          Journal:  J Cell Biol        ISSN： 0021-9525            Impact factor:   10.539


  32 in total

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Journal:  Eur J Biochem       Date:  1979-10

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Journal:  Biochim Biophys Acta       Date:  1973-01-25

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Journal:  J Biochem       Date:  1967-11       Impact factor: 3.387

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Journal:  Cell       Date:  1975-11       Impact factor: 41.582

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Journal:  Nature       Date:  1981-12-10       Impact factor: 49.962

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Authors:  M Koenig; A P Monaco; L M Kunkel
Journal:  Cell       Date:  1988-04-22       Impact factor: 41.582

10.  The Duchenne muscular dystrophy gene product is localized in sarcolemma of human skeletal muscle.

Authors:  E E Zubrzycka-Gaarn; D E Bulman; G Karpati; A H Burghes; B Belfall; H J Klamut; J Talbot; R S Hodges; P N Ray; R G Worton
Journal:  Nature       Date:  1988-06-02       Impact factor: 49.962
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  13 in total

1.  Isolated dystrophin molecules as seen by electron microscopy.

Authors:  F Pons; N Augier; R Heilig; J Léger; D Mornet; J J Léger
Journal:  Proc Natl Acad Sci U S A       Date:  1990-10       Impact factor: 11.205

2.  Monoclonal antibodies for dystrophin analysis. Epitope mapping and improved binding to SDS-treated muscle sections.

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Journal:  Biochem J       Date:  1992-12-01       Impact factor: 3.857

Review 3.  The structure and function of alpha-actinin.

Authors:  A Blanchard; V Ohanian; D Critchley
Journal:  J Muscle Res Cell Motil       Date:  1989-08       Impact factor: 2.698

4.  Heterogeneity of dystrophin expression in patients with Duchenne and Becker muscular dystrophy.

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Journal:  Acta Neuropathol       Date:  1990       Impact factor: 17.088

5.  Developmental expression of spectrins in rat skeletal muscle.

Authors:  D Zhou; J A Ursitti; R J Bloch
Journal:  Mol Biol Cell       Date:  1998-01       Impact factor: 4.138

6.  Use of epitope libraries to identify exon-specific monoclonal antibodies for characterization of altered dystrophins in muscular dystrophy.

Authors:  T M Nguyen; G E Morris
Journal:  Am J Hum Genet       Date:  1993-06       Impact factor: 11.025

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Authors:  L L Lien; F M Boyce; P Kleyn; L M Brzustowicz; J Menninger; D C Ward; T C Gilliam; L M Kunkel
Journal:  Proc Natl Acad Sci U S A       Date:  1991-09-01       Impact factor: 11.205

8.  Localization of the DMDL gene-encoded dystrophin-related protein using a panel of nineteen monoclonal antibodies: presence at neuromuscular junctions, in the sarcolemma of dystrophic skeletal muscle, in vascular and other smooth muscles, and in proliferating brain cell lines.

Authors:  T M Nguyen; J M Ellis; D R Love; K E Davies; K C Gatter; G Dickson; G E Morris
Journal:  J Cell Biol       Date:  1991-12       Impact factor: 10.539

9.  Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated with the sarcoplasmic reticulum of mammalian skeletal muscle.

Authors:  D Zhou; C S Birkenmeier; M W Williams; J J Sharp; J E Barker; R J Bloch
Journal:  J Cell Biol       Date:  1997-02-10       Impact factor: 10.539

10.  Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma.

Authors:  K Ohlendieck; J M Ervasti; J B Snook; K P Campbell
Journal:  J Cell Biol       Date:  1991-01       Impact factor: 10.539
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